ID PDE4E_DROME Reviewed; 662 AA.
AC Q8IRU4;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-APR-2013, entry version 81.
DE RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase, isoform F;
DE EC=3.1.4.17;
DE AltName: Full=Learning/memory process protein;
DE AltName: Full=Protein dunce;
GN Name=dnc; ORFNames=CG32498;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a
RT systematic review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
CC -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
CC regulator of many important physiological processes (By
CC similarity). Vital for female fertility. Required for
CC learning/memory (By similarity).
CC -!- CATALYTIC ACTIVITY: Adenosine 3',5'-cyclic phosphate + H(2)O =
CC adenosine 5'-phosphate.
CC -!- COFACTOR: Binds 2 divalent metal cations per subunit. Site 1 may
CC preferentially bind zinc ions, while site 2 has a preference for
CC magnesium and/or manganese ions (By similarity).
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Name=F;
CC IsoId=Q8IRU4-1; Sequence=Displayed;
CC Note=No experimental confirmation available;
CC Name=G;
CC IsoId=Q9W4S9-2; Sequence=External;
CC Note=No experimental confirmation available;
CC Name=I; Synonyms=B, O;
CC IsoId=Q9W4T4-1; Sequence=External;
CC Name=II; Synonyms=I, J;
CC IsoId=P12252-1; Sequence=External;
CC Name=III; Synonyms=E;
CC IsoId=P12252-7; Sequence=External;
CC Note=Produced by alternative initiation at Met-429 of isoform
CC II;
CC Name=IV; Synonyms=A;
CC IsoId=P12252-3; Sequence=External;
CC Name=V; Synonyms=C;
CC IsoId=P12252-4; Sequence=External;
CC Name=VI; Synonyms=D;
CC IsoId=P12252-5; Sequence=External;
CC Name=VII; Synonyms=L;
CC IsoId=P12252-6; Sequence=External;
CC Name=M;
CC IsoId=Q9W4T0-1; Sequence=External;
CC Note=No experimental confirmation available;
CC Name=N;
CC IsoId=Q9W4S9-1; Sequence=External;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
CC family. PDE4 subfamily.
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DR EMBL; AE014298; AAN09606.1; -; Genomic_DNA.
DR RefSeq; NP_525061.2; NM_080322.3.
DR UniGene; Dm.4817; -.
DR ProteinModelPortal; Q8IRU4; -.
DR SMR; Q8IRU4; 144-178, 253-574.
DR PRIDE; Q8IRU4; -.
DR EnsemblMetazoa; FBtr0070521; FBpp0070497; FBgn0000479.
DR GeneID; 31309; -.
DR KEGG; dme:Dmel_CG32498; -.
DR UCSC; CG32498-RA; d. melanogaster.
DR CTD; 31309; -.
DR FlyBase; FBgn0000479; dnc.
DR GeneTree; ENSGT00690000101692; -.
DR InParanoid; Q8IRU4; -.
DR KO; K01120; -.
DR UniPathway; UPA00762; UER00747.
DR ChiTaRS; dnc; drosophila.
DR GenomeRNAi; 31309; -.
DR NextBio; 772953; -.
DR Bgee; Q8IRU4; -.
DR GermOnline; CG32498; Drosophila melanogaster.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048675; P:axon extension; IMP:FlyBase.
DR GO; GO:0048149; P:behavioral response to ethanol; NAS:FlyBase.
DR GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019933; P:cAMP-mediated signaling; NAS:FlyBase.
DR GO; GO:0001661; P:conditioned taste aversion; IMP:FlyBase.
DR GO; GO:0007619; P:courtship behavior; TAS:FlyBase.
DR GO; GO:0046331; P:lateral inhibition; IMP:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; NAS:FlyBase.
DR GO; GO:0046958; P:nonassociative learning; TAS:FlyBase.
DR GO; GO:0008355; P:olfactory learning; TAS:FlyBase.
DR GO; GO:0048477; P:oogenesis; TAS:FlyBase.
DR GO; GO:0007614; P:short-term memory; IMP:FlyBase.
DR GO; GO:0007268; P:synaptic transmission; IMP:FlyBase.
DR Gene3D; 1.10.1300.10; -; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR023174; PDEase_CS.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR PROSITE; PS00126; PDEASE_I; 1.
PE 3: Inferred from homology;
KW Alternative splicing; cAMP; Complete proteome; Hydrolase;
KW Metal-binding; Reference proteome.
FT CHAIN 1 662 cAMP-specific 3',5'-cyclic
FT phosphodiesterase, isoform F.
FT /FTId=PRO_0000198820.
FT NP_BIND 324 328 cAMP (By similarity).
FT ACT_SITE 324 324 Proton donor (By similarity).
FT METAL 328 328 Divalent metal cation 1 (By similarity).
FT METAL 364 364 Divalent metal cation 1 (By similarity).
FT METAL 365 365 Divalent metal cation 1 (By similarity).
FT METAL 365 365 Divalent metal cation 2 (By similarity).
FT METAL 482 482 Divalent metal cation 1 (By similarity).
FT BINDING 365 365 cAMP (By similarity).
FT BINDING 482 482 cAMP (By similarity).
FT BINDING 533 533 cAMP (By similarity).
FT SITE 485 485 Binds AMP, but not cAMP (By similarity).
SQ SEQUENCE 662 AA; 72954 MW; D195C7DAFCBD3CC3 CRC64;
MLNKNSASSQ SLPRVHSFFN MIPSIMQDDL ALTILNDRDN MFSIKSQRSH GEDLIVTPFA
QILASLRSVR NNLLSLTNVP ASNKSRRPNQ SSSASRSGNP PGAPLSQGEE AYTRLATDTI
EELDWCLDQL ETIQTHRSVS DMASLKFKRM LNKELSHFSE SSRSGNQISE YICSTFLDKQ
QEFDLPSLRV EDNPELVAAN AAAGQQSAGQ YARSRSPRGP PMSQISGVKR PLSHTNSFTG
ERLPTFGVET PRENELGTLL GELDTWGIQI FSIGEFSVNR PLTCVAYTIF QSRELLTSLM
IPPKTFLNFM STLEDHYVKD NPFHNSLHAA DVTQSTNVLL NTPALEGVFT PLEVGGALFA
ACIHDVDHPG LTNQFLVNSS SELALMYNDE SVLENHHLAV AFKLLQNQGC DIFCNMQKKQ
RQTLRKMVID IVLSTDMSKH MSLLADLKTM VETKKVAGSG VLLLDNYTDR IQVLENLVHC
ADLSNPTKPL PLYKRWVALL MEEFFLQGDK ERESGMDISP MCDRHNATIE KSQVGFIDYI
VHPLWETWAD LVHPDAQDIL DTLEENRDYY QSMIPPSPPP SGVDENPQED RIRFQVTLEE
SDQENLAELE EGDESGGEST TTGTTGTTAA SALSGAGGGG GGGGGMAPRT GGCQNQPQHG
GM
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